Research workbench
The structure of the arabidopsis thaliana guanosine deaminase mutant Y185F complexed with guanosine
Analyse The structure of the arabidopsis thaliana guanosine deaminase mutant Y185F… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DQN
- Type
- protein
- Length
- 313 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanosine deaminase
- EC
- 3.5.4.15
- UniProt
- Q94BU8
- Ligands
- GMP, ZN
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanosine deaminase (EC 3.5.4.15) | protein | 157 | 43% helix, 17% strand | Q94BU8 |
| D | Guanosine deaminase (EC 3.5.4.15) | protein | 156 | 44% helix, 19% strand | Q94BU8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.77 | 0.95 | 25 | GMP |
| 2 | 209 | 0.65 | 0.84 | 28 | empty |
| 3 | 61 | 0.29 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–D · 1598 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 7DQN · The structure of the Arabidopsis thaliana guanosine deaminase mutant Y185F complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q94BU8 · AlphaFold monomer V2.0 prediction for guanosine deaminase (Q94BU8) · a predicted model of the same protein · chain A against A, TM-score 0.94
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q94BU8
- Elsewhere: RCSB PDB 7DQN · PDBe 7DQN · UniProt Q94BU8
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